Difference between revisions of "Part:BBa K283036"

Latest revision as of 12:18, 21 October 2009

invasin(1-625aa)

The invasin protein of Yersinia pseudotuberculosis has been utilized for heterologous surface display. Y. pseudotuberculosis invasin promotes bacterial entry by binding to host cell integrins. It is a 986-residue protein of which the 500 N-terminal aa are thought to reside in the outer membrane. The C-terminal 497 residues, which make up the extracellular part, are involved in the binding to integrin. Nakajima and co-workers developed a system for expression of random peptides on the cell surface of E. coli by creation of a fusion hybrid between a peptide and the invasin protein. This part can be used to display fusion protein on the surface of bacteria. This part does not pose any biological threat.

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
COMPATIBLE WITH RFC[21]
23
COMPATIBLE WITH RFC[23]
25
INCOMPATIBLE WITH RFC[25]
Illegal AgeI site found at 886
1000
COMPATIBLE WITH RFC[1000]

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 <partinfo>BBa_K283036 short</partinfo>
-The invasin protein of ''Yersinia pseudotuberculosis'' has been utilized for heterologous surface display. ''Y. pseudotuberculosis'' invasin promotes bacterial entry by binding to host cell integrins. It is a 986-residue protein of which the  500 N-terminal aa are thought to reside in the outer membrane. The C-terminal 497 residues, which make up the extracellular part, are involved in the binding to integrin. Nakajima and co-workers developed a system for expression of random peptides on the cell surface of ''E. coli'' by creation of a fusion hybrid between a peptide and the invasin protein. This part can be used to display fusion protein on the surface of bacteria.
+The invasin protein of ''Yersinia pseudotuberculosis'' has been utilized for heterologous surface display. ''Y. pseudotuberculosis'' invasin promotes bacterial entry by binding to host cell integrins. It is a 986-residue protein of which the  500 N-terminal aa are thought to reside in the outer membrane. The C-terminal 497 residues, which make up the extracellular part, are involved in the binding to integrin. Nakajima and co-workers developed a system for expression of random peptides on the cell surface of ''E. coli'' by creation of a fusion hybrid between a peptide and the invasin protein. This part can be used to display fusion protein on the surface of bacteria. This part does not pose any biological threat.
 <!-- Add more about the biology of this part here